Laparoscopic resection of two peritoneal loose bodies on the rectosigmoid colon

Laparoscopic examination of a 77-year-old woman revealed two peritoneal loose bodies connected to fatty appendices on the rectosigmoid colon and resected at the stalks. The peritoneal loose bodies were found to be fat-containing masses on preoperative magnetic resonance imaging, and postoperative pathological examination revealed fat degeneration tissue with or without fibrous outer layers

Novel COL5A2 mutation in Ehlers–Danlos syndrome

Ehlers–Danlos syndrome (EDS) is a group of inherited connective tissue disorders characterized by hyperextensible skin, joint hypermobility and soft tissue fragility. For molecular diagnosis, targeted exome sequencing was performed on a 9-year-old male patient who was clinically suspected to have EDS. The patient presented with progressive kyphoscoliosis, joint hypermobility and hyperextensible skin without scars. Ultimately, classical EDS was diagnosed by identifying a novel, mono-allelic mutation in COL5A2 [NM_000393.3(COL5A2_v001):c.682G>A, p.Gly228Arg]

Novel CHD7 mutation in CHARGE syndrome

CHARGE syndrome is a rare autosomal dominant developmental disorder involving multiple organs. CHD7 is a major causative gene of CHARGE syndrome. We performed targeted-exome sequencing using a next-generation sequencer for molecular diagnosis of a 4-month-old male patient who was clinically suspected to have CHARGE syndrome, and report a novel monoallelic mutation in CHD7, NM_017780.3(CHD7_v001):c.2966del causing a reading frameshift [p.(Cys989Serfs*3)]

Lowe syndrome caused by gloss deletion

Lowe syndrome (LS) is an X-linked disorder affecting the eyes, nervous system and kidneys, typically caused by missense or nonsense/frameshift OCRL mutations. We report a 6-month-old male clinically suspected to have LS, but without the Fanconi-type renal dysfunction. Using a targeted-exome sequencing-first approach, LS was diagnosed by the identification of a deletion involving 1.7 Mb at Xq25-q26.1, encompassing the entire OCRL gene and neighboring loci

マリアナ弧北端部の熱水活動域（日光海山）より単離した新規Epsilon-Proteobacteriaの諸性質

BE09-P99ポスター要旨 / ブルーアース2009（2009年3月12日～13日, 立教大学池袋キャンパス）http://www.godac.jamstec.go.jp/darwin/cruise/natsushima/nt05-18/

RBM10 in complete hydatidiform mole: cytoplasmic occurrence of its 50 kDa polypeptide

Background: RNA-binding motif protein 10 (RBM10), originally identified as S1-1 protein, is a nuclear protein with likely functions in transcription and RNA splicing. The RBM10 gene maps to the X chromosome and, in female cells, is inactivated in one of the two X chromosomes near the boundary with genes escaping inactivation. This study investigated the occurrence of the RBM10 gene product in complete hydatidiform mole, which is composed of cells with paternal diploid chromosomes (46, XX).Methods: Deparaffinized normal chorion or complete hydatidiform mole tissues were hybridized with a fluorescein-conjugated RBM10 gene probe in fluorescent in situ hybridization (FISH) analysis. Immunohistochemistry and immunoelectron microscopy of the tissues were performed using an anti-RBM10 antiserum. Proteins from complete hydatidiform mole tissues and those separated by anti-RBM10-linked affinity chromatography were also examined by western blotting.Results: As expected, the RBM10 gene was detected by FISH as double spots in the nuclei of complete hydatidiform mole cells. Immunohistochemistry revealed a nuclear presence of RBM10 in normal chorion and complete hydatidiform moles, and a notable cytoplasmic presence in complete hydatidiform moles. Western blotting and immunoaffinity chromatography revealed that a 50 kDa protein was predominantly found in the cytosolic fraction of complete hydatidiform moles.Conclusions: A 50 kDa protein with common antigenicity to RBM10 was found in the cytoplasm of complete hydatidiform mole cells, and could represent one of the characteristics of the disease

The crystal structure of the plant small GTPase OsRac1 reveals its mode of binding to NADPH oxidase

This research was originally published in Journal of Biological Chemistry. Ken-ichi Kosami, Izuru Ohki, Minoru Nagano, Kyoko Furuita, Toshihiko Sugiki, Yoji Kawano, Tsutomu Kawasaki, Toshimichi Fujiwara, Atsushi Nakagawa, Ko Shimamoto and Chojiro Kojima. The crystal structure of the plant small GTPase OsRac1 reveals its mode of binding to NADPH oxidase. Journal of Biological Chemistry. 2014; 289, 28569-28578. © the American Society for Biochemistry and Molecular Biology